Rickettsia Lipid A Biosynthesis Utilizes the Late Acyltransferase LpxJ for Secondary Fatty Acid Addition

Journal of Bacteriology
Mark L GuillotteAbdu F Azad

Abstract

Members of the Rickettsia genus are obligate intracellular, Gram-negative coccobacilli that infect mammalian and arthropod hosts. Several rickettsial species are human pathogens and are transmitted by blood-feeding arthropods. In Gram-negative parasites, the outer membrane (OM) sits at the nexus of the host-pathogen interaction and is rich in lipopolysaccharide (LPS). The lipid A component of LPS anchors the molecule to the bacterial surface and is an endotoxic agonist of Toll-like receptor 4 (TLR4). Despite the apparent importance of lipid A in maintaining OM integrity, as well as its inflammatory potential during infection, this molecule is poorly characterized in Rickettsia pathogens. In this work, we have identified and characterized new members of the recently discovered LpxJ family of lipid A acyltransferases in both Rickettsia typhi and Rickettsia rickettsii, the etiological agents of murine typhus and Rocky Mountain spotted fever, respectively. Our results demonstrate that these enzymes catalyze the addition of a secondary acyl chain (C14/C16) to the 3'-linked primary acyl chain of the lipid A moiety in the final steps of the Raetz pathway of lipid A biosynthesis. Since lipid A architecture is fundamental to bacterial O...Continue Reading

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Citations

Nov 6, 2020·Biotechnology and Applied Biochemistry·Qing ZhouXiaoyuan Wang
Oct 6, 2020·FEMS Microbiology Reviews·Edgardo Moreno
Mar 7, 2021·International Journal of Molecular Sciences·Kazuyoshi Kawahara
May 7, 2021·MSphere·Mark L GuillotteAbdu F Azad

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Datasets Mentioned

BETA
AAU03534

Methods Mentioned

BETA
acylation

Software Mentioned

MUSCLE
BLAST
WebLogo
blastp
Phyre2
flexAnalysis
R

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